ID A0A166V7J9_9PEZI Unreviewed; 884 AA.
AC A0A166V7J9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Quinate repressor (Shikimate dehydrogenase substrate binding domain-containing protein) {ECO:0000313|EMBL:KZL74262.1};
GN ORFNames=CT0861_05623 {ECO:0000313|EMBL:KZL74262.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL74262.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL74262.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL74262.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: In the 2nd section; belongs to the type-I 3-dehydroquinase
CC family. {ECO:0000256|ARBA:ARBA00006477}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the shikimate kinase
CC family. {ECO:0000256|ARBA:ARBA00009349}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZL74262.1}.
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DR EMBL; LFIV01000034; KZL74262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166V7J9; -.
DR STRING; 708197.A0A166V7J9; -.
DR OrthoDB; 2256238at2759; -.
DR Proteomes; UP000076552; Unassembled WGS sequence.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:InterPro.
DR CDD; cd00502; DHQase_I; 1.
DR CDD; cd01065; NAD_bind_Shikimate_DH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR031322; Shikimate/glucono_kinase.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21090; AROM/DEHYDROQUINATE SYNTHASE; 1.
DR PANTHER; PTHR21090:SF27; QUINATE REPRESSOR PROTEIN; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR Pfam; PF01202; SKI; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076552}.
FT DOMAIN 542..622
FT /note="Shikimate dehydrogenase substrate binding N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08501"
FT DOMAIN 684..726
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 827..855
FT /note="SDH C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18317"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 97651 MW; 98A832E556FD66DF CRC64;
MATAGVKRSY VATAMNDDED HRHQLENPAK FVRVDARNGH SASPSQPQSP RTNSSRYSMA
ACSRPETPVT RPATPISHLP GEVPPFPADA SIVLAGIRGA GKSTLAIIAS TAMERRAVDC
EKAFQQVTGL TSFAYKRAHG PVECHRRQTD VLRDLLDQSA KNTLIVCSWM ERGVQTLLRD
FCRTHPVIHI IRDVKAIQEH LKIEDDDKAR NLLAASSTIF RTCSNLEFFN VSETADPWVE
TDAARIEAQA GGQKLPAPYL TLKRAERHFL KFLSLIMPKG SIPFIESAFP LASIPTEDRR
FTYAISVSLS SLLNNELAIE ELETGADAIE IVVDGIAGAT PLDSERAADI ARIIGSIRRS
TVIPLMYHVV LPDSSESVYM DYILHGLRLS PEYLTVDLRL NDYQLLHIIS MKRRSKIIGH
LTPAVDSPSW GDPFWMSHYH RARRLGCDLV RLIKPVTSIK DNFDINHLKA LVDASAGHKI
PLIAYNSGPR GRHSAAMNHV LTSVVPEPMA STYNPNQPCL TAVQATQALY NSFLFDPMKM
YVFGAHVSYS LSPAMHNAAL KACGIPHIYR PFSTPSLNGL RELIEDPYFA GASVGLPFKV
EIITLTHSLS RHAQAIGAVN TLVPVRRLNP DGTIPEDEKL FNCRNRAGPV RALYGENTDW
IGIRACIRRG LSPANAVRTT SCGLIIGAGG MARAATYSML QLGVKNIVVY NRTIANAEKM
VNHFTRLLTR HDLPLLSATS DVGTRFHIVR SLDEPWPEDF RLPTMIVSCI PTHSIGDVPA
PNFIAPQAWL GSPTGGCLVE LGYKTLDTPI LNQARQVSHR GWVTMDGLDL LPEQGFAQFE
LFTGRRAPRR LMRGEVFRAY PDGQDRSALA QLQPRLNNIV EQEP
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